Canmetcon
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Identification
YMDB IDYMDB00104
NameL-Homoserine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionL-Homoserine is an alpha-amino acid. L-Homoserine is derived from L-aspartate in the homoserine biosynthesis pathway. It is the precursor in homocysteine biosynthesis pathway and in threonine biosynthesis from homoserine pathway. In certain organisms, including the yeast Saccharomyces cerevisiae S288c and certain bacteria, hydrogen sulfide reacts with O-acetyl-L-homoserine, replacing the acetyl group and forming L-homocysteine. [Biocyc HOMOSERSYN-PWY and PWY-5344 and HOMOSER-THRESYN-PWY]
Structure
Thumb
Synonyms
  • (S)-2-amino-4-hydroxy-Butanoate
  • (S)-2-amino-4-hydroxy-Butanoic acid
  • (S)-2-Amino-4-hydroxybutanoate
  • (S)-2-Amino-4-hydroxybutanoic acid
  • (S)-Homoserine
  • 2-amino-4-hydroxy-Butyrate
  • 2-amino-4-hydroxy-Butyric acid
  • 2-amino-4-hydroxy-L-Butyrate
  • 2-amino-4-hydroxy-L-Butyric acid
  • 2-Amino-4-hydroxybutanoate
  • 2-Amino-4-hydroxybutanoic acid
  • 2-Amino-4-hydroxybutyrate
  • 2-Amino-4-hydroxybutyric acid
  • Homoserine
  • L-Homoserine
  • (2S)-2-Amino-4-hydroxybutanoic acid
  • (2S)-2-Amino-4-hydroxybutanoate
  • Homoserine L-isomer
  • L Isomer OF homoserine
  • L-Isomer OF homoserine
CAS number672-15-1
WeightAverage: 119.1192
Monoisotopic: 119.058243159
InChI KeyUKAUYVFTDYCKQA-VKHMYHEASA-N
InChIInChI=1S/C4H9NO3/c5-3(1-2-6)4(7)8/h3,6H,1-2,5H2,(H,7,8)/t3-/m0/s1
IUPAC Name(2S)-2-amino-4-hydroxybutanoic acid
Traditional IUPAC NameL-homoserine
Chemical FormulaC4H9NO3
SMILES[H]OC(=O)[C@@]([H])(N([H])[H])C([H])([H])C([H])([H])O[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentL-alpha-amino acids
Alternative Parents
Substituents
  • L-alpha-amino acid
  • Short-chain hydroxy acid
  • Fatty acid
  • 1,3-aminoalcohol
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Organic oxide
  • Primary amine
  • Primary alcohol
  • Organooxygen compound
  • Organonitrogen compound
  • Organopnictogen compound
  • Primary aliphatic amine
  • Organic oxygen compound
  • Carbonyl group
  • Amine
  • Alcohol
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point203 °C
Experimental Properties
PropertyValueReference
Water Solubility1000 mg/mL at 30 oC [BEILSTEIN]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility423 g/LALOGPS
logP-3.3ALOGPS
logP-3.8ChemAxon
logS0.55ALOGPS
pKa (Strongest Acidic)2.22ChemAxon
pKa (Strongest Basic)9.16ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area83.55 ŲChemAxon
Rotatable Bond Count3ChemAxon
Refractivity26.91 m³·mol⁻¹ChemAxon
Polarizability11.44 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Cysteine MetabolismPW002383 ThumbThumb?image type=greyscaleThumb?image type=simple
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
Sulfur metabolismPW002483 ThumbThumb?image type=greyscaleThumb?image type=simple
threonine metabolismPW002401 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Glycine, serine and threonine metabolismec00260 Map00260
Lysine biosynthesisec00300 Map00300
Sulfur metabolismec00920 Map00920
SMPDB Reactions
L-Homoserine + Acetyl-CoACoenzyme A + Acetylhomoserine
NADPH + L-aspartic 4-semialdehyde + hydronL-Homoserine + NADP
L-aspartic 4-semialdehyde + hydron + NADPHNADP + L-Homoserine
L-Homoserine + Adenosine triphosphateADP + hydron + O-Phosphohomoserine
KEGG Reactions
NADH + L-aspartic 4-semialdehyde + hydronNAD + L-Homoserine
L-aspartic 4-semialdehyde + NADPH + hydronNADP + L-Homoserine
Adenosine triphosphate + L-Homoserinehydron + O-Phosphohomoserine + ADP
Acetyl-CoA + L-HomoserineCoenzyme A + O-Acetyl-L-homoserine
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Wiebers, J. L., Garner, H. R. (1967). "Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli." J Biol Chem 242:5644-5649.12325384
  • Robichon-Szulmajster, H., Cherest, H. (1967). "Regulation of homoserine O-transacetylase, first step in methionine biosyntheis in Saccharomyces cerevisiae." Biochem Biophys Res Commun 28:256-262.6035500
  • Cherest, H., Eichler, F., Robichon-Szulmajster, H. (1969). "Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae." J Bacteriol 97:328-336.5764336
  • Huo, X., Viola, R. E. (1996). "Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli." Biochemistry 35:16180-16185.8973190
  • Kosuge, T., Gao, D., Hoshino, T. (2000). "Analysis of the methionine biosynthetic pathway in the extremely thermophilic eubacterium Thermus thermophilus." J Biosci Bioeng 90:271-279.16232856
  • Thomas, D., Barbey, R., Surdin-Kerjan, Y. (1993). "Evolutionary relationships between yeast and bacterial homoserine dehydrogenases." FEBS Lett 323:289-293.8500624
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Kokusenya, Yoshio; Matsuoka, Manabu. Synthesis of amino acids by electrochemical reduction. I. Synthesis of L-homoserine by electrochemical reduction of L-asparagine. Denki Kagaku oyobi Kogyo Butsuri Kagaku (1987), 55(2), 174-5.
External Links:
ResourceLink
CHEBI ID15699
HMDB IDHMDB00719
Pubchem Compound ID12647
Kegg IDC00263
ChemSpider ID12126
FOODB IDFDB000521
WikipediaHomoserine
BioCyc IDHOMO-SER

Enzymes

General function:
Involved in O-acetyltransferase activity
Specific function:
Acetyl-CoA + L-homoserine = CoA + O-acetyl-L- homoserine
Gene Name:
MET2
Uniprot ID:
P08465
Molecular weight:
53659.0
Reactions
Acetyl-CoA + L-homoserine → CoA + O-acetyl-L-homoserine.
General function:
Involved in ATP binding
Specific function:
Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate
Gene Name:
THR1
Uniprot ID:
P17423
Molecular weight:
38712.0
Reactions
ATP + L-homoserine → ADP + O-phospho-L-homoserine.
General function:
Involved in amino acid binding
Specific function:
ATP + L-aspartate = ADP + 4-phospho-L- aspartate
Gene Name:
HOM3
Uniprot ID:
P10869
Molecular weight:
58109.19922
Reactions
ATP + L-aspartate → ADP + 4-phospho-L-aspartate.
General function:
Involved in oxidoreductase activity
Specific function:
L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Gene Name:
HOM6
Uniprot ID:
P31116
Molecular weight:
38501.69922
Reactions
L-homoserine + NAD(P)(+) → L-aspartate 4-semialdehyde + NAD(P)H.